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Katarína uchov Nikolaj Spodsberg Kristian B. R. Mrkeberg Krogh Peter Biely Vladimír Puchart 《Molecules (Basel, Switzerland)》2021,26(15)
This study describes the catalytic properties of a GH30_7 xylanase produced by the fungus Talaromyces leycettanus. The enzyme is an ando-β-1,4-xylanase, showing similar specific activity towards glucuronoxylan, arabinoxylan, and rhodymenan (linear β-1,3-β-1,4-xylan). The heteroxylans are hydrolyzed to a mixture of linear as well as branched β-1,4-xylooligosaccharides that are shorter than the products generated by GH10 and GH11 xylanases. In the rhodymenan hydrolyzate, the linear β-1,4-xylooligosaccharides are accompanied with a series of mixed linkage homologues. Initial hydrolysis of glucuronoxylan resembles the action of other GH30_7 and GH30_8 glucuronoxylanases, resulting in a series of aldouronic acids of a general formula MeGlcA2Xyln. Due to the significant non-specific endoxylanase activity of the enzyme, these acidic products are further attacked in the unbranched regions, finally yielding MeGlcA2Xyl2-3. The accommodation of a substituted xylosyl residue in the −2 subsite also applies in arabinoxylan depolymerization. Moreover, the xylose residue may be arabinosylated at both positions 2 and 3, without negatively affecting the main chain cleavage. The catalytic properties of the enzyme, particularly the great tolerance of the side-chain substituents, make the enzyme attractive for biotechnological applications. The enzyme is also another example of extraordinarily great catalytic diversity among eukaryotic GH30_7 xylanases. 相似文献
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A thermophilic microorganism growing within the temperature range of 40–65 °C (optimum at 55 °C) was isolated from hot water
springs near Konkan, Maharashtra, India. Based on 16S rDNA sequence analysis, it was concluded that the isolate belongs to
the genus Brevibacillus. The present paper reports the isolation, identification, and standardization of fermentation conditions for the production
of enzyme, bile salt hydrolase (EC 3.5.1.24) which is produced intracellularly at high temperatures. This is the first report
regarding the production of bile salt hydrolase from a thermophilic source. Optimization of fermentation conditions resulted
in a 2.9-fold enhancement in enzyme production. 相似文献